| + |
MMP7 | down-regulates quantity by destabilization 
cleavage
|
DCN |
0.59 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256352 |
Glu273 |
ANTPHLReLHLDNNK |
in vitro |
|
| pmid |
sentence |
| 9148753 |
Degradation of decorin by matrix metalloproteinases. These data indicate proteolytic degradation of DCN by MMP-2, MMP-3 and MMP-7, and suggest the possibility that, under pathophysiological conditions, the digestion by the MMPs may induce tissue reactions mediated by TGF-beta1 released from DCN in the connective tissues. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256351 |
Glu30 |
GLFDFMLeDEASGIG |
in vitro |
|
| pmid |
sentence |
| 9148753 |
Degradation of decorin by matrix metalloproteinases. These data indicate proteolytic degradation of DCN by MMP-2, MMP-3 and MMP-7, and suggest the possibility that, under pathophysiological conditions, the digestion by the MMPs may induce tissue reactions mediated by TGF-beta1 released from DCN in the connective tissues. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
MMP7 | down-regulates quantity by destabilization
cleavage
|
HAPLN1 |
0.327 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256329 |
Leu40 |
QAENGPHlLVEAEQA |
in vitro |
|
| pmid |
sentence |
| 7694569 |
Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein. Sequencing studies of modified link protein components revealed that stromelysins-1 and -2, gelatinases A and B and collagenase cleaved specifically between His16 and Ile17, and matrilysin, stromelysin-2 and gelatinase A cleaved between Leu25 and Leu26. Based on previously determined in situ cleavage sites it is evident that matrix metalloproteinases are not solely responsible for the accumulation of link protein degradation products in adult human cartilage, indicating that additional proteolytic agents are involved in the normal catabolism of human cartilage matrix. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MMP7 | up-regulates activity 
cleavage
|
SPP1 |
0.693 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253321 |
|
|
|
|
| pmid |
sentence |
| 25545242 |
In this study, we found a novel motif, LRSKSRSFQVSDEQY, in the C-terminal fragment of MMP-3/7-cleaved mouse OPN binds to α9β1 integrin. Importantly, this novel motif is involved in the development of anti-type II collagen antibody-induced arthritis (CAIA). This study provides the first in vitro and in vivo evidence that OPN cleavage by MMP-3/7 is an important regulatory mechanism for CAIA. |
|
| Publications: |
1 |
| + |
MMP7 | up-regulates 
|
ECM_disassembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272374 |
|
|
|
|
| pmid |
sentence |
| 17318226 |
Historically, MMPs were thought to function mainly as enzymes that degrade structural components of the ECM. |
|
| Publications: |
1 |
| + |
MMP7 | down-regulates 
|
ECM |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272397 |
|
|
|
|
| pmid |
sentence |
| 17318226 |
Historically, MMPs were thought to function mainly as enzymes that degrade structural components of the ECM. |
|
| Publications: |
1 |
3.0
MMP7
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